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| PROSITE documentation PDOC00788 |
Dehydroquinase class I active site
Description:
3-dehydroquinate dehydratase (EC 4.2.1.10), or dehydroquinase, catalyzes the
conversion of 3-dehydroquinate into 3-dehydroshikimate. It is the third step
in the shikimate pathway for the biosynthesis of aromatic amino acids from
chorismate. Two classes of dehydroquinases exist, known as types I and II. The
best studied type I enzyme is from Escherichia coli (gene aroD) and related
bacteria where it is a homodimeric protein of a chain of about 250 residues.
In fungi, dehydroquinase is part of a multifunctional enzyme which catalyzes
five consecutive steps in the shikimate pathway. In aroD, it has been shown
[1] that a histidine is involved in the catalytic mechanism; we used the
region around this residue as a signature pattern.
Last update:
December 2001 / Pattern and text revised.
Technical section:
PROSITE method (with tools and information) covered by this documentation:
| DEHYDROQUINASE_I, PS01028; Dehydroquinase class I active site (PATTERN) |
| Consensus pattern: |
D-[LIVM]-[DE]-[LIVMN]-x(18,20)-[LIVM](2)-x-[SC]-[NHY]-H-[DN]
H is the active site residue |
| Sequences known to belong to this class detected by the pattern: |
ALL |
| Other sequence(s) detected in Swiss-Prot: |
NONE |
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| Matching PDB structures:
1GQN 1L9W 1QFE 2EGZ ... [ALL] |
Reference:
| 1 |
Authors | Deka R.K., Kleanthous C., Coggins J.R. |
| Title | Identification of the essential histidine residue at the active site of Escherichia coli dehydroquinase. |
| Source | J. Biol. Chem. 267:22237-22242(1992). |
| PubMed ID | 1429576 |
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